Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue.
The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism.
Scott
D L
DL
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Otwinowski
Z
Z
Gelb
M H
MH
Sigler
P B
PB
D000595:Amino Acid Sequence; D001514:Bee Venoms / Q000032:analysis*; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D050260:Carbohydrate Metabolism; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D010741:Phospholipases A / Q000737:chemistry* / Q000378:metabolism; D054467:Phospholipases A2; D011487:Protein Conformation
D001514:Bee Venoms; D010714:Phosphatidylethanolamines; C066847:1-O-octyl-2-heptylphosphonylglycero-3-phosphoethanolamine; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium